Nitta Hidetoshi, Kobayashi Hidetomo, Irie Atsushi, Baba Hideo, Okamoto Keinosuke, Imamura Takahisa
Department of Molecular Pathology, Faculty of Medical and Pharmaceutical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto 860-8556, Japan.
FEBS Lett. 2007 Dec 22;581(30):5935-9. doi: 10.1016/j.febslet.2007.11.076. Epub 2007 Dec 5.
The effect of a serine protease (ASP) secreted from Aeromonas sobria on plasma coagulation was investigated. Proteolytically active ASP promoted human plasma coagulation in a dose-dependent manner. Consistent with the preference for a factor Xa-specific oligo-peptide substrate, ASP produced enzymatic activity from human prothrombin but not from factors IX and X. ASP cleaved prothrombin to produce enzymatically active 37 kDa-fragment displaying the same molecular mass as alpha-thrombin. ASP is the first bacterial serine protease that produces alpha-thrombin, through which ASP may contribute to the induction of thrombotic tendency in disseminated intravascular coagulation complicated with sepsis caused by A. sobria infections.
研究了温和气单胞菌分泌的一种丝氨酸蛋白酶（ASP）对血浆凝固的影响。具有蛋白水解活性的ASP以剂量依赖方式促进人血浆凝固。与对Xa因子特异性寡肽底物的偏好一致，ASP可使人凝血酶原产生酶活性，但不能使IX因子和X因子产生酶活性。ASP切割凝血酶原以产生具有酶活性的37 kDa片段，其分子量与α-凝血酶相同。ASP是第一种产生α-凝血酶的细菌丝氨酸蛋白酶，通过它ASP可能在由温和气单胞菌感染引起的败血症并发的弥散性血管内凝血中促成血栓形成倾向的诱导。
